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Protein

Molybdopterin synthase catalytic subunit

Gene

moaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.

Miscellaneous

The cross-link is not seen in all structures of the MoaE-MoaD complex.

Catalytic activityi

Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein].1 Publication

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei119SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processMolybdenum cofactor biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11598-MONOMER
MetaCyc:EG11598-MONOMER
BRENDAi2.8.1.12 2026
UniPathwayiUPA00344

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin synthase catalytic subunit (EC:2.8.1.12)
Alternative name(s):
MPT synthase subunit 2
Molybdenum cofactor biosynthesis protein E
Molybdopterin-converting factor large subunit
Molybdopterin-converting factor subunit 2
Gene namesi
Name:moaE
Synonyms:chlA5
Ordered Locus Names:b0785, JW0768
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11598 moaE

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34F → A: 4-fold lower activity than wild-type. 1 Publication1
Mutagenesisi39R → A: 24-fold lower activity than wild-type. 1 Publication1
Mutagenesisi115M → A: 4-fold lower activity than wild-type. 1 Publication1
Mutagenesisi119K → A: No activity. 1 Publication1
Mutagenesisi126K → A: 58-fold lower activity than wild-type. Accumulates large quantities of reaction intermediate. 1 Publication1
Mutagenesisi128E → K: 17-fold lower activity than wild-type. 1 Publication1
Mutagenesisi140R → A: 2-fold lower activity than wild-type. 1 Publication1

Chemistry databases

DrugBankiDB01942 Formic Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001630822 – 150Molybdopterin synthase catalytic subunitAdd BLAST149

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in MoaD)

Keywords - PTMi

Isopeptide bond

Proteomic databases

PaxDbiP30749
PRIDEiP30749

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also stable as homodimer. The enzyme changes between these two forms during catalysis.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4262180, 17 interactors
DIPiDIP-10232N
IntActiP30749, 21 interactors
STRINGi316385.ECDH10B_0853

Structurei

Secondary structure

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Helixi15 – 22Combined sources8
Beta strandi30 – 37Combined sources8
Beta strandi50 – 54Combined sources5
Helixi56 – 73Combined sources18
Beta strandi76 – 84Combined sources9
Beta strandi86 – 88Combined sources3
Beta strandi93 – 103Combined sources11
Helixi104 – 121Combined sources18
Beta strandi124 – 130Combined sources7
Beta strandi133 – 136Combined sources4
Helixi141 – 148Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FM0X-ray1.45E1-150[»]
1FMAX-ray1.58E1-150[»]
1NVIX-ray1.90E1-150[»]
1NVJX-ray2.15A/B/C/D/E/F1-140[»]
3BIIX-ray2.50E2-150[»]
ProteinModelPortaliP30749
SMRiP30749
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30749

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 39Substrate bindingBy similarity3
Regioni103 – 104Substrate bindingBy similarity2
Regioni126 – 128Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the MoaE family.Curated

Phylogenomic databases

eggNOGiENOG4108ZAF Bacteria
COG0314 LUCA
HOGENOMiHOG000280876
InParanoidiP30749
KOiK03635
OMAiWKKEMYE
PhylomeDBiP30749

Family and domain databases

CDDicd00756 MoaE, 1 hit
Gene3Di3.90.1170.40, 1 hit
InterProiView protein in InterPro
IPR036563 MoaE_sf
IPR003448 Mopterin_biosynth_MoaE
PfamiView protein in Pfam
PF02391 MoaE, 1 hit
SUPFAMiSSF54690 SSF54690, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETKIVVGP QPFSVGEEYP WLAERDEDGA VVTFTGKVRN HNLGDSVNAL
60 70 80 90 100
TLEHYPGMTE KALAEIVDEA RNRWPLGRVT VIHRIGELWP GDEIVFVGVT
110 120 130 140 150
SAHRSSAFEA GQFIMDYLKT RAPFWKREAT PEGDRWVEAR ESDQQAAKRW
Length:150
Mass (Da):16,981
Last modified:January 23, 2007 - v3
Checksum:i6E40776E5A6E85BB
GO

Mass spectrometryi

Molecular mass is 16849.7±0.7 Da from positions 2 - 150. Determined by ESI. 1 Publication
Molecular mass is 16851 Da from positions 2 - 150. Determined by API. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA Translation: CAA49865.1
U00096 Genomic DNA Translation: AAC73872.1
AP009048 Genomic DNA Translation: BAA35443.1
PIRiS35002 S31883
RefSeqiNP_415306.1, NC_000913.3
WP_000852296.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73872; AAC73872; b0785
BAA35443; BAA35443; BAA35443
GeneIDi945399
KEGGiecj:JW0768
eco:b0785
PATRICifig|1411691.4.peg.1493

Similar proteinsi

Entry informationi

Entry nameiMOAE_ECOLI
AccessioniPrimary (citable) accession number: P30749
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 153 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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